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Appl. Environ. Microbiol. doi:10.1128/AEM.01446-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum

Institute for Biotechnology and Biomedicine, Department of Genetics and Microbiology, Autonomous University of Barcelona, and CIBER de Bioingeniería, Biomateriales y Nanomedicina (CIBER-BBN), Spain, Bellaterra, 08193 Barcelona, Spain

^* To whom correspondence should be addressed. Email: avillaverde{at}servet.uab.es.

	Abstract

We have observed that a soluble recombinant GFP produced in E. coli occurs in a wide conformational spectrum. This fact results in differently fluorescent protein fractions in which morphologically diverse soluble aggregates abound. Therefore, the functional quality of soluble versions of aggregation-prone recombinant proteins is defined statistically rather than by a canonical native structure.